PL EN


Preferencje help
Widoczny [Schowaj] Abstrakt
Liczba wyników
2009 | 14 | 4 |

Tytuł artykułu

The anti-apoptotic activity of albumin for endothelium is inhibited by advanced glycation and products restricting intramolecular movement

Warianty tytułu

Języki publikacji

EN

Abstrakty

EN
Human serum albumin (HSA) inhibits endothelial apoptosis in a highly specific manner. CNBr fragmentation greatly increases the effectiveness of this activity, suggesting that this type of protection is mediated by a partially cryptic albumin domain which is transiently exposed by intramolecular movement. Advanced glycation end-product (AGE) formation in HSA greatly reduces its intra-molecular movement. This study aimed to determine if this inhibits the anti-apoptotic activity of HSA, and if such inactivation could be reversed by CNBr fragmentation. HSA-AGE was prepared by incubating HSA with glucose, and assessed using the fructosamine assay, mass spectrometry, SDS-PAGE and fluorometry. Low levels of AGE in the HSA had little effect upon its anti-apoptotic activity, but when the levels of AGE were high and the intra-molecular movement was reduced, endothelial cell survival was also found to be reduced to levels equivalent to those in cultures without HSA or serum (p > 0.001). Survival was restored by the inclusion of native HSA, despite the presence of HSA with high levels of AGE. Also, CNBr fragmentation of otherwise inactive HSA-AGE restored the anti-apoptotic activity for endothelium. Apoptosis was confirmed by DNA gel electrophoresis, transmission electron microscopy and fluorescence-activated cell sorting analysis, and there was no evidence for direct toxicity in the HSA-AGE preparations. The results are consistent with the proposed role of intra-molecular movement in exposing the anti-apoptotic domain in HSA for endothelium. The levels of AGE formation required to inhibit the anti-apoptotic activity of HSA exceeded those reported for diabetes. Nonetheless, the data from this study seems to be the first example of reduced protein function due to AGE-restricted intra-molecular movement.

Wydawca

-

Rocznik

Tom

14

Numer

4

Opis fizyczny

p.575-586,fig.,ref.

Twórcy

autor
  • The University of Sydney, Westmead, NSW 2145, Australia
autor
autor
autor

Bibliografia

  • 1. Araki, S., Shimada, Y., Kaji, K. and Hayashi, H. Role of protein kinase C in the inhibition by fibroblast growth factor of apoptosis in serum-deprived endothelial cells. Biochem. Biophys. Res. Commun. 172 (1990) 1081- 1085.
  • 2. Zoellner, H., Hou, J.Y., Lovery, M., Kingham, J., Srivastava, M., Bielek, E., Vanyek, E. and Binder, B.R. Inhibition of microvascular endothelial apoptosis in tissue explants by serum albumin. Microvasc. Res. 57 (1999) 162-173.
  • 3. Zoellner, H., Hofler, M., Beckmann, R., Hufnagl, P., Vanyek, E., Bielek, E., Wojta, J., Fabry, A., Lockie, S. and Binder, B.R. Serum albumin is a specific inhibitor of apoptosis in human endothelial cells. J. Cell Sci. 109 (1996) 2571-2580.
  • 4. Bolitho, C., Bayl, P., Hou, J.Y., Lynch, G., Hassel, A.J., Wall, A.J. and Zoellner, H. The anti-apoptotic activity of albumin for endothelium is mediated by a partially cryptic protein domain and reduced by inhibitors of G-coupled protein and PI-3 kinase, but is independent of radical scavenging or bound lipid. J. Vasc. Res. 44 (2007) 313-324.
  • 5. Djousse, L., Rothman, K.J., Cupples, L.A., Levy, D. and Ellison, R.C. Serum albumin and risk of myocardial infarction and all-cause mortality in the Framingham Offspring Study. Circulation 106 (2002) 2919-2924.
  • 6. Schillinger, M., Exner, M., Mlekusch, W., Amighi, J., Sabeti, S., Schlager, O., Wagner, O. and Minar, E. Serum albumin predicts cardiac adverse events in patients with advanced atherosclerosis - interrelation with traditional cardiovascular risk factors. Thromb. Haemost. 91 (2004) 610-618.
  • 7. Peters, T. All about albumin - biochemistry, genetics and medical applications. San Diego, Academic Press, 1996.
  • 8. Zoellner, H., Hou, J.Y., Hochgrebe, T., Poljak, A., Duncan, M.W., Golding, J., Henderson, T. and Lynch, G. Fluorometric and mass spectrometric analysis of nonenzymatic glycosylated albumin. Biochem. Biophys. Res. Commun. 284 (2001) 83-89.
  • 9. Brownlee, M., Vlassara, H. and Cerami, A. Nonenzymatic glycosylation and the pathogenesis of diabetic complications. Ann. Intern. Med. 101 (1984) 527-537.
  • 10. John, W.G. and Lamb, E.J. The Maillard or browning reaction in diabetes. Eye 7 ( Pt 2) (1993) 230-237.
  • 11. Drickamer, K. Diabetes: Breaking the curse of the AGEs. Nature 382 (1996) 211-212.
  • 12. Lee, A.T. and Cerami, A. Role of glycation in aging. Ann. N. Y. Acad. Sci. 663 (1992) 63-70.
  • 13. Ahmed, M.U., Thorpe, S.R. and Baynes, J.W. Identification of N epsiloncarboxymethyllysine as a degradation product of fructoselysine in glycated protein. J. Biol. Chem. 261 (1986) 4889-4894.
  • 14. Wolff, S.P., Jiang, Z.Y. and Hunt, J.V. Protein glycation and oxidative stress in diabetes mellitus and ageing. Free Radic. Biol. Med. 10 (1991) 339-352.
  • 15. Johnson, R.N., Metcalf, P.A. and Baker, J.R. Fructosamine: a new approach to the estimation of serum glycosylprotein. An index of diabetic control. Clin. Chim. Acta 127 (1983) 87-95.
  • 16. Emmanuel, C., Foo, E., Medbury, H., Matthews, J., Comis, A. and Zoellner, H. Synergistic induction of apoptosis in human endothelial cells by tumor necrosis factor-α and transforming growth factor-β. Cytokine 18 (2002) 237-241.
  • 17. Smith, C.A., Williams, G.T., Kingston, R., Jenkinson, E.J. and Owen, J.J. Antibodies to CD3/T-cell receptor complex induce death by apoptosis in immature T-cells in thymic cultures. Nature 337 (1989) 181-184.
  • 18. Darzynkiewicz, Z., Bruno, S., Del Bino, G., Gorczyca, W., Hotz, M.A., Lassota, P. and Traganos, F. Features of apoptotic cells measured by flow cytometry. Cytometry 13 (1992) 795-808.
  • 19. Gerschenson, L.E. and Rotello, R.J. Apoptosis: a different type of cell death. FASEB J. 6 (1992) 2450-2455.
  • 20. Raff, M.C., Barres, B.A., Burne, J.F., Coles, H.S., Ishizaki, Y. and Jacobson, M.D. Programmed cell death and the control of cell survival: lessons from the nervous system. Science 262 (1993) 695-700.
  • 21. Kumar, V., Abbas, A.K., Fausto, N. Robbins and Cotran Pathologic Basis of Disease. Philadelphia, W.B. Saunders Co., 2004.
  • 22. Zoellner, H., Bielek, E., Vanyek, E., Fabry, A., Wojta, J., Hofler, M. and Binder, B.R. Canalicular fragmentation of apoptotic human endothelial cells. Endothelium 4 (1996) 177-188.
  • 23. Xu, W., Boadle, R., Dear, L., Cvejic, M., Emmanuel, C. and Zoellner, H. Ultrastructural changes in endothelium during apoptosis indicate low microembolic potential. J. Vasc. Res. 42 (2005) 377-387.
  • 24. Chibber, R., Molinatti, P.A., Rosatto, N., Lambourne, B. and Kohner, E.M. Toxic action of advanced glycation end products on cultured retinal capillary pericytes and endothelial cells: relevance to diabetic retinopathy. Diabetologia 40 (1997) 156-164.
  • 25. Min, C., Kang, E., Yu, S., Shinn, S. and Kim, Y. Advanced glycation end products induce apoptosis and procoagulant activity in cultured human umbilical vein endothelial cells. Diabetes Res. Clin. Pract. 46 (1999) 197-202.
  • 26. Kowluru, R.A. Effect of advanced glycation end products on accelerated apoptosis of retinal capillary cells under in vitro conditions. Life Sci. 76 (2005) 1051-1060.
  • 27. Xiang, M., Yang, M., Zhou, C., Liu, J., Li, W. and Qian, Z. Crocetin prevents AGEs-induced vascular endothelial cell apoptosis. Pharmacol. Res. 54 (2006) 268-274.
  • 28. Stefani, M. Protein misfolding and aggregation: new examples in medicine and biology of the dark side of the protein world. Biochim. Biophys. Acta 1739 (2004) 5-25.
  • 29. Cantara, S., Ziche, M. and Donnini, S. Opposite effects of beta amyloid on endothelial cell survival: role of fibroblast growth factor-2 (FGF-2). Pharmacol. Rep. 57 Suppl (2005) 138-143.
  • 30. Cecchi, C., Pensalfini, A., Baglioni, S., Fiorillo, C., Caporale, R., Formigli, L., Liguri, G. and Stefani, M. Differing molecular mechanisms appear to underlie early toxicity of prefibrillar HypF-N aggregates to different cell types. FEBS J. 273 (2006) 2206-2222.
  • 31. Bouma, B., Kroon-Batenburg, L.M., Wu, Y.P., Brunjes, B., Posthuma, G., Kranenburg, O., de Groot, P.G., Voest, E.E. and Gebbink, M.F. Glycation induces formation of amyloid cross-beta structure in albumin. J. Biol. Chem. 278 (2003) 41810-41819.
  • 32. Rondeau, P., Singh, N.R., Caillens, H., Tallet, F., and Bourdon, E. Oxidative stress induced by glycoxidized human or bovine serum albumin on human monocytes. Free Radic. Biol. Med. 45 (2008) 799-812.
  • 33. Hunt, J.V., Bottoms, M.A., and Mitchinson, M.J. Oxidative alterations in experimental glycation model of diabetes mellitus are due to protein-glucose adduct oxidation. Some fundamental differences in proposed mechanisms of glucose oxidation and oxidant production. Biochem. J. 291 (1993) 529-535.
  • 34. Darby, I.A., Bisucci, T., Hewitson, T.D. and MacLellan, D.G. Apoptosis is increased in a model of diabetes-impaired wound healing in genetically diabetic mice. Int. J. Biochem. Cell Biol. 29 (1997) 191-200.
  • 35. Mizutani, M., Kern, T.S. and Lorenzi, M. Accelerated death of retinal microvascular cells in human and experimental diabetic retinopathy. J. Clin. Invest. 97 (1996) 2883-2890.
  • 36. Thornalley, P.J., Argirova, M., Ahmed, N., Mann, V.M., Argirov, O. and Dawnay, A. Mass spectrometric monitoring of albumin in uremia. Kidney Int. 58 (2000) 2228-2234.

Typ dokumentu

Bibliografia

Identyfikatory

Identyfikator YADDA

bwmeta1.element.agro-article-6978cbe3-a8e8-4425-b507-4b3305454ea1
JavaScript jest wyłączony w Twojej przeglądarce internetowej. Włącz go, a następnie odśwież stronę, aby móc w pełni z niej korzystać.